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The objective of the present study was to determine whether angiotensinogen G(–6)A polymorphism is associated with the elevation of blood pressure (BP) in the hypertensive disorders of pregnancy in Korean population. The subjects included 201 cases with the hypertensive disorders of pregnancy and 160 healthy controls. The medical records of subjects were reviewed. Cases were classified into the four subtypes (transient hypertension, preeclampsia, chronic hypertension, and preeclampsia superimposed on chronic hypertension) by the diagnostic criteria suggested by the National High Blood Pressure Education Program Working Group. Cases were also divided into the high and low BP group by the elevation of BP (diastolic BP greater than or equal to 110 mmHg). Maternal angiotensinogen G(–6)A polymorphism was determined by restriction fragment length polymorphism. Frequencies of AA genotype were significantly higher in the high than in the low BP group in the preeclampsia, superimposed preeclampsia, and the combined group (N = 201), suggesting that the angiotensinogen G(–6)A allele was significantly associated with the elevation of BP in the hypertensive disorders of pregnancy among South Korean women. The present findings imply that the elevation of BP can serve as an endophenotype for a spectrum of hypertensive conditions in pregnancy.
Recombinant human αs1-casein expressed
in Escherichia coli was purified
and digested with trypsin in an attempt to find peptides with angiotensin-I-converting enzyme (ACE) inhibitory activity. Three novel ACE inhibitory peptides,
A-II, B-II and C, were isolated and their amino acid sequences identified as
Tyr–Pro–Glu–Arg (residues 8–11),
136–143) and Asn–Asn–Val–Met–Leu–Gln–Trp
(residues 164–170) respectively. ACE
inhibitory activities were measured for the corresponding synthetic peptides, and the
ACE IC50 (the amount of peptide causing 50% inhibition of ACE activity) values of
A-II, B-II and C estimated to be 132·5, 24·8 and 41·0 μmol/l respectively. Peptides
A-II and C were resistant to further digestion by pepsin, whereas peptide B-II was
hydrolysed. All three peptides were resistant to digestion by chymotrypsin. These
ACE inhibitory peptides may prove useful for oral administration in the treatment
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